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Probing Temperature- and pH-Dependent Binding between Quantum Dots and Bovine Serum Albumin by Fluorescence Correlation Spectroscopy

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Laboratory of Fiber Materials and Modern Textile, The Growing Base for State Key Laboratory, College of Chemistry and Chemical Engineering, Shandong Sino-Japanese Center for Collaborative Research of Carbon Nanomaterials, Collaborative Innovation Center for Marine Biomass Fiber Materials and Textiles, Qingdao University, Qingdao 266071, China
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CAS Key Laboratory of Standardization and Measurement for Nanotechnology, CAS Center for Excellence in Nanoscience, National Center for Nanoscience and Technology, Beijing 100190, China
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Laboratory for Biological Effects of Nanomaterials and Nanosafety, National Center for Nanoscience and Technology, Beijing 100190, China
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University of Chinese Academy of Sciences, Beijing 100049, China
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School of Life Sciences and Biotechnology, Shanghai Jiao Tong University, Shanghai 200240, China
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Shanghai Center for Systems Biomedicine, Shanghai Jiao Tong University, Shanghai 200240, China
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Authors to whom correspondence should be addressed.
Academic Editor: Kevin Critchley
Nanomaterials 2017, 7(5), 93; https://doi.org/10.3390/nano7050093
Received: 13 March 2017 / Revised: 15 April 2017 / Accepted: 21 April 2017 / Published: 25 April 2017
(This article belongs to the Special Issue Quantum Dots for Following Therapeutic Delivery)
Luminescent quantum dots (QDs) with unique optical properties have potential applications in bio-imaging. The interaction between QDs and bio-molecules is important to the biological effect of QDs in vivo. In this paper, we have employed fluorescence correlation spectroscopy (FCS) to probe the temperature- and pH-dependent interactions between CdSe QDs with carboxyl (QDs-COOH) and bovine serum albumin (BSA) in buffer solutions. The results have shown that microscopic dissociation constant K′D is in the range of (1.5 ± 0.2) × 10−5 to (8.6 ± 0.1) × 10−7 M, the Hill coefficient n is from 0.4 to 2.3, and the protein corona thickness is from 3.0 to 9.4 nm. Variable-temperature measurements have shown both negative values of ∆H and ∆S for BSA adsorption on QDs-COOH, while pH has a profound effect on the adsorption. Additional, FCS measurement QDs-COOH and proteins in whole mice serum and plasma samples has also been conducted. Finally, simulation results have shown four favored QD binding sites in BSA. View Full-Text
Keywords: luminescent quantum dots; fluorescence correlation spectroscopy; temperature-and pH-dependent interactions; simulation luminescent quantum dots; fluorescence correlation spectroscopy; temperature-and pH-dependent interactions; simulation
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MDPI and ACS Style

Wang, Z.; Zhao, Q.; Cui, M.; Pang, S.; Wang, J.; Liu, Y.; Xie, L. Probing Temperature- and pH-Dependent Binding between Quantum Dots and Bovine Serum Albumin by Fluorescence Correlation Spectroscopy. Nanomaterials 2017, 7, 93. https://doi.org/10.3390/nano7050093

AMA Style

Wang Z, Zhao Q, Cui M, Pang S, Wang J, Liu Y, Xie L. Probing Temperature- and pH-Dependent Binding between Quantum Dots and Bovine Serum Albumin by Fluorescence Correlation Spectroscopy. Nanomaterials. 2017; 7(5):93. https://doi.org/10.3390/nano7050093

Chicago/Turabian Style

Wang, Zonghua, Qiyan Zhao, Menghua Cui, Shichao Pang, Jingfang Wang, Ying Liu, and Liming Xie. 2017. "Probing Temperature- and pH-Dependent Binding between Quantum Dots and Bovine Serum Albumin by Fluorescence Correlation Spectroscopy" Nanomaterials 7, no. 5: 93. https://doi.org/10.3390/nano7050093

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